Severity: Warning
Message: file_get_contents(https://...@gmail.com&api_key=61f08fa0b96a73de8c900d749fcb997acc09&a=1): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests
Filename: helpers/my_audit_helper.php
Line Number: 197
Backtrace:
File: /var/www/html/application/helpers/my_audit_helper.php
Line: 197
Function: file_get_contents
File: /var/www/html/application/helpers/my_audit_helper.php
Line: 271
Function: simplexml_load_file_from_url
File: /var/www/html/application/helpers/my_audit_helper.php
Line: 3165
Function: getPubMedXML
File: /var/www/html/application/controllers/Detail.php
Line: 597
Function: pubMedSearch_Global
File: /var/www/html/application/controllers/Detail.php
Line: 511
Function: pubMedGetRelatedKeyword
File: /var/www/html/index.php
Line: 317
Function: require_once
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Mass spectrometric data obtained using a model of tandem carotid artery stenosis in mice with unstable and stable atherosclerosis were analyzed to identify differences in the level of post-translational modifications (PTMs) of proteins. The original proteomic data obtained by Chen et al. [DOI: 10.1038/s42003-023-04641-4] and deposited in the PRIDE repository (identifier PXD030857) were used. Based on results of the bioinformatic analysis, 12 proteins with PTMs (methylation, acetylation, and phosphorylation) were selected; comparison of healthy and atherosclerotic vascular sections showed that the selected proteins were characterized by significant changes in the level of individual modified peptides. According to the literature data, all 12 proteins are involved in the process of atherogenesis. Our study thus revealed putative points of regulation of the atherogenesis processes at the PTM level.
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http://dx.doi.org/10.18097/PBMCR1575 | DOI Listing |